Fig. 5: Conformational behaviour of O-linked oligosaccharides bound in the active site of HvExoI calculated by cMD simulations plotted as a function of θ and φ puckering coordinates. | Nature Communications

Fig. 5: Conformational behaviour of O-linked oligosaccharides bound in the active site of HvExoI calculated by cMD simulations plotted as a function of θ and φ puckering coordinates.

From: The evolutionary advantage of an aromatic clamp in plant family 3 glycoside exo-hydrolases

Fig. 5

a Sophorose (G2OG; pink); b laminaribiose (G3OG; magenta); c cellotriose (G4OG4OG; cyan); and d gentiobiose (G6OG; green) ligands are bound at the −1 to +2 subsites (colour gradients from purple at 0 ns to yellow at 200 ns in Mercator projections are indicated). Complexes of WT with G3SG,  G4SG4OG, G6SG, and W434A in complex with G2SG were used to predict binding modes of O-linked oligosaccharides. The β-d-glucopyranose moieties at the −1 to +2 subsites, and dispositions of Asp285 and Glu491 catalytic residues are also shown.

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